A novel mechanism for substrate inhibition in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase

Journal of Biological Chemistry

Volumn 282, Issue 43, 2007, Pages 31517-31524

  Burton, Rodney L ^a   Chen, Shawei ^a   Xiao, Lan Xu ^a   Grant, Gregory A ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HYDROXYPYRUVIC ACID PHOSPHATE; OPTIMAL SUBSTRATE INHIBITION; SUBSTRATE INHIBITION;

BACTERIA; CONCENTRATION (PROCESS); DISEASES; ESTERS; MUTAGENESIS; PH EFFECTS; SUBSTRATES;

ENZYME KINETICS;

AMINO ACID; ANION; BACTERIAL ENZYME; DEXTRO 3 PHOSPHOGLYCERATE DEHYDROGENASE; HYDROXYPYRUVIC ACID PHOSPHATE; PYRUVIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; ENZYME ACTIVITY; LIGAND BINDING; MUTAGENESIS; MYCOBACTERIUM TUBERCULOSIS; PH; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE;

ALLOSTERIC REGULATION; AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HYDROGEN BONDING; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PHOSPHOGLYCERATE DEHYDROGENASE; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PYRUVIC ACID; SUBSTRATE SPECIFICITY;

MYCOBACTERIUM TUBERCULOSIS;

EID: 35748973899     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M704032200     Document Type: Article

References (15)

1. Dey, S., Hu, Z., Xu, X. L., Sacchettini, J. C., and Grant, G. A. (2005) J. Biol. Chem. 280, 14884-14891
2. Dey, S., Grant, G. A., and Sacchettini, J. C. (2005) J. Biol. Chem. 280, 14892-14899
3. Schuller, D., Grant, G. A., and Banaszak, L. (1995) Nat. Struct. Biol. 2, 69-76
4. Aravind, L., and Koonin, E. V. (1999) J. Mol. Biol. 287, 1023-1040
5. Chipman, D. M., and Shaanan, B. (2001) Curr. Opin. Struct. Biol. 11, 694-700
6. Grant, G. A. (2006) J. Biol. Chem. 281, 33825-33829
7. Sassetti, C. M., Boyd, D. H., and Rubin, E. J. (2003) Mol. Microbiol. 48, 77-84
8. Sugimoto, E., and Pizer, L. I. (1968) J. Biol. Chem. 243, 2081
9. Cormack, B. (1991) in Current Protocols in Molecular Biology (Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., eds) pp. 8.5.1-8.5.9, John Wiley and Sons, New York
10. LiCata, V. J., and Allewell, N. M. (1997) Biophys. Chem. 64, 225-234
11. Cleland, W. (1979) Methods Enzymol. 63, 500-513
12. Segel, I. H. (1975) Enzyme Kinetics, pp. 818-826, Wiley Interscience, New York
13. Achouri, Y., Rider, M. H., Van Schaftingen, E., and Robbi, M. (1997) Biochem. J. 323, 365-370
14. Russell, D. G. (2007) Nat. Rev. Microbiol. 5, 39-47
15. Honer zu Bentrup, K., and Russell, D. G. (2001) Trends Microbiol. 9, 597-605